CREB-bindingseiwit

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Het CREB-bindingseiwit

Het CREB-bindingseiwit (CREB-Binding-Protein, afgekort CBP), is een co-activator bij de transcriptie.

Bij de mens wordt het CREB-bindingseiwit gecodeerd door het CREBBP-gen (ook wel CBP-gen genoemd).[1][2]

Het CREB-bindingseiwit heeft de volgende domeinen:

De CREB-bindingseiwit domeinen, KIX, TAZ1 en TAZ2 binden elk stevig aan de beide transactivatie domeinen 9aaTADs van de transcriptiefactor p53.[3][4]

Functie[bewerken]

Het CREBBP-gen is betrokken bij de transcriptionele co-activatie van veel verschillende transcriptiefactoren. Het werd voor het eerst geïsoleerd als een nucleuseiwit dat zich bindt aan het cAMP-reactie-elementbindend eiwit (CREB). Het gen speelt een kritische rol bij de embryonale ontwikkeling, controle van de groei en homeostase door te koppelen aan chromatine en het zo geschikt te maken voor de herkenning van de transcriptiefactor. Het door het gen gecodeerde eiwit heeft een eigen histon-acetyltransferase activiteit [5] en werkt ook ondersteunend voor het stabiliseren van bijkomende eiwitinteracties met het transcriptieomplex. Het eiwit acetyleert zowel histonen als non-histon eiwitten. Het eiwit heeft zeer sterk vergelijkbare regio's met het eiwit EP300 en hun bromodomein, cysteïne-histidine-rijke regio's en het histonacetyltransferasedomein.[6]

Klinisch belang[bewerken]

Mutaties in het CREBBP-gen is de oorzaak van het Rubinstein-taybisyndroom (RTS).[7] De chromosomale translocatie, waarbij het CREBBP-gen betrokken is, wordt in verband gebracht met acute myeloïde leukemie.[6][8]

Interacties[bewerken]

Het CREB-bindingseiwit vertoont interactie met de volgende eiwitten:

Bronnen, noten en/of referenties
  1. Chrivia JC, Kwok RP, Lamb N, Hagiwara M, Montminy MR, Goodman RH (October 1993). Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 365 (6449): 855–9 . PMID:8413673. DOI:10.1038/365855a0.
  2. Wydner KL, Bhattacharya S, Eckner R, Lawrence JB, Livingston DM (November 1995). Localization of human CREB-binding protein gene (CREBBP) to 16p13.2-p13.3 by fluorescence in situ hybridization. Genomics 30 (2): 395–6 . PMID:8586450.
  3. Teufel DP, Freund SM, Bycroft M, Fersht AR (April 2007). Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. PNAS 104 (17): 7009–7014 . PMID:17438265. PMC:1855428. DOI:10.1073/pnas.0702010104.; Piskacek S, Gregor M, Nemethova M, Grabner M, Kovarik P, Piskacek M (June 2007). Nine-amino-acid transactivation domain: establishment and prediction utilities. Genomics 89 (6): 756–68 . PMID:17467953. DOI:10.1016/j.ygeno.2007.02.003.; Piskacek M (2009-11-05). 9aaTAD is a common transactivation domain recruits multiple general coactivators TAF9, MED15, CBP/p300 and GCN5. Nature Precedings Pre-publication . DOI:10.1038/npre.2009.3488.2.; Piskacek M (2009-11-05). 9aaTADs mimic DNA to interact with a pseudo-DNA Binding Domain KIX of Med15 (Molecular Chameleons). Nature Precedings Pre-publication . DOI:10.1038/npre.2009.3939.1.; Piskacek M (2009-11-20). 9aaTAD Prediction result (2006). Nature Precedings Pre-publication . DOI:10.1038/npre.2009.3984.1.
  4. The prediction for 9aaTADs (for both acidic and hydrophilic transactivation domains) is available online from ExPASy http://us.expasy.org/tools/ and EMBnet Spain http://www.es.embnet.org/Services/EMBnetAT/htdoc/9aatad/
  5. Ogryzko VV et al. "The transcriptional coactivators p300 and CBP are histone acetyltransferases". Cell. 1996 87(5):953-9.[1]
  6. a b Entrez Gene: CREBBP (CREB-binding protein)
  7. Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RC, Masuno M, Tommerup N, van Ommen GJ, Goodman RH, Peters DJ (July 1995). Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature 376 (6538): 348–51 . PMID:7630403. DOI:10.1038/376348a0.
  8. Vizmanos JL, Larráyoz MJ, Lahortiga I, Floristán F, Alvarez C, Odero MD, Novo FJ, Calasanz MJ (April 2003). t(10;16)(q22;p13) and MORF-CREBBP fusion is a recurrent event in acute myeloid leukemia. Genes Chromosomes Cancer 36 (4): 402–5 . PMID:12619164. DOI:10.1002/gcc.10174.
  9. a b c Sano, Y, Tokitou F, Dai P, Maekawa T, Yamamoto T, Ishii S (Oct. 1998). CBP alleviates the intramolecular inhibition of ATF-2 function. J. Biol. Chem. 273 (44): 29098–105 (UNITED STATES)​. ISSN:0021-9258. PMID:9786917. DOI:10.1074/jbc.273.44.29098.
  10. a b Kim, J, Jia L, Stallcup M R, Coetzee G A (Feb. 2005). The role of protein kinase A pathway and cAMP responsive element-binding protein in androgen receptor-mediated transcription at the prostate-specific antigen locus. J. Mol. Endocrinol. 34 (1): 107–18 (England)​. ISSN:0952-5041. PMID:15691881. DOI:10.1677/jme.1.01701.
  11. Frønsdal, K, Engedal N, Slagsvold T, Saatcioglu F (Nov. 1998). CREB binding protein is a coactivator for the androgen receptor and mediates cross-talk with AP-1. J. Biol. Chem. 273 (48): 31853–9 (UNITED STATES)​. ISSN:0021-9258. PMID:9822653. DOI:10.1074/jbc.273.48.31853.
  12. Ishitani, Ken, Yoshida Tasuku, Kitagawa Hirochika, Ohta Hiroaki, Nozawa Shiro, Kato Shigeaki (Jul. 2003). p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor. Biochem. Biophys. Res. Commun. 306 (3): 660–5 (United States)​. ISSN:0006-291X. PMID:12810069. DOI:10.1016/S0006-291X(03)01021-0.
  13. a b Aarnisalo, P, Palvimo J J, Jänne O A (Mar. 1998). CREB-binding protein in androgen receptor-mediated signaling. Proc. Natl. Acad. Sci. U.S.A. 95 (5): 2122–7 (UNITED STATES)​. ISSN:0027-8424. PMID:9482849. PMC:19270. DOI:10.1073/pnas.95.5.2122.
  14. Pitkänen, J, Doucas V, Sternsdorf T, Nakajima T, Aratani S, Jensen K, Will H, Vähämurto P, Ollila J, Vihinen M, Scott H S, Antonarakis S E, Kudoh J, Shimizu N, Krohn K, Peterson P (Jun. 2000). The autoimmune regulator protein has transcriptional transactivating properties and interacts with the common coactivator CREB-binding protein. J. Biol. Chem. 275 (22): 16802–9 (UNITED STATES)​. ISSN:0021-9258. PMID:10748110. DOI:10.1074/jbc.M908944199.
  15. Iioka, Takashi, Furukawa Keizo, Yamaguchi Akira, Shindo Hiroyuki, Yamashita Shunichi, Tsukazaki Tomoo (Aug. 2003). P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain. J. Bone Miner. Res. 18 (8): 1419–29 (United States)​. ISSN:0884-0431. PMID:12929931. DOI:10.1359/jbmr.2003.18.8.1419.
  16. a b c Fan, Saijun, Ma Yong Xian, Wang Chenguang, Yuan Ren-Qi, Meng Qinghui, Wang Ji-An, Erdos Michael, Goldberg Itzhak D, Webb Paul, Kushner Peter J, Pestell Richard G, Rosen Eliot M (Jan. 2002). p300 Modulates the BRCA1 inhibition of estrogen receptor activity. Cancer Res. 62 (1): 141–51 (United States)​. ISSN:0008-5472. PMID:11782371.
  17. Pao, G M, Janknecht R, Ruffner H, Hunter T, Verma I M (Feb. 2000). CBP/p300 interact with and function as transcriptional coactivators of BRCA1. Proc. Natl. Acad. Sci. U.S.A. 97 (3): 1020–5 (UNITED STATES)​. ISSN:0027-8424. PMID:10655477. PMC:15508. DOI:10.1073/pnas.97.3.1020.
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  23. Kovacs KA, Steinmann M, Magistretti PJ, Halfon O, Cardinaux JR (Sept. 2003). CCAAT/enhancer-binding protein family members recruit the coactivator CREB-binding protein and trigger its phosphorylation. J Biol. Chem. 278 (38): 36959–65 (UNITED STATES)​. ISSN:0021-9258. PMID:12857754. DOI:10.1074/jbc.M303147200.
  24. Lorentz, O, Suh E R, Taylor J K, Boudreau F, Traber P G (Mar. 1999). CREB-binding [corrected] protein interacts with the homeodomain protein Cdx2 and enhances transcriptional activity. J. Biol. Chem. 274 (11): 7196–9 (UNITED STATES)​. ISSN:0021-9258. PMID:10066780. DOI:10.1074/jbc.274.11.7196.
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  26. Shimomura, A, Ogawa Y, Kitani T, Fujisawa H, Hagiwara M (Jul. 1996). Calmodulin-dependent protein kinase II potentiates transcriptional activation through activating transcription factor 1 but not cAMP response element-binding protein. J. Biol. Chem. 271 (30): 17957–60 (UNITED STATES)​. ISSN:0021-9258. PMID:8663317. DOI:10.1074/jbc.271.30.17957.
  27. Radhakrishnan, I, Pérez-Alvarado G C, Parker D, Dyson H J, Montminy M R, Wright P E (Dec. 1997). Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91 (6): 741–52 (UNITED STATES)​. ISSN:0092-8674. PMID:9413984. DOI:10.1016/S0092-8674(00)80463-8.
  28. a b Zor, Tsaffrir, Mayr Bernhard M, Dyson H Jane, Montminy Marc R, Wright Peter E (Nov. 2002). Roles of phosphorylation and helix propensity in the binding of the KIX domain of CREB-binding protein by constitutive (c-Myb) and inducible (CREB) activators. J. Biol. Chem. 277 (44): 42241–8 (United States)​. ISSN:0021-9258. PMID:12196545. DOI:10.1074/jbc.M207361200.
  29. a b Giebler, H A, Lemasson I, Nyborg J K (Jul. 2000). p53 recruitment of CREB binding protein mediated through phosphorylated CREB: a novel pathway of tumor suppressor regulation. Mol. Cell. Biol. 20 (13): 4849–58 (UNITED STATES)​. ISSN:0270-7306. PMID:10848610. PMC:85936. DOI:10.1128/MCB.20.13.4849-4858.2000.
  30. a b Zhang, Q, Vo N, Goodman R H (Jul. 2000). Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB. Mol. Cell. Biol. 20 (14): 4970–8 (UNITED STATES)​. ISSN:0270-7306. PMID:10866654. PMC:85947. DOI:10.1128/MCB.20.14.4970-4978.2000.
  31. a b Ernst, P, Wang J, Huang M, Goodman R H, Korsmeyer S J (Apr. 2001). MLL and CREB bind cooperatively to the nuclear coactivator CREB-binding protein. Mol. Cell. Biol. 21 (7): 2249–58 (United States)​. ISSN:0270-7306. PMID:11259575. PMC:86859. DOI:10.1128/MCB.21.7.2249-2258.2001.
  32. Ledo, Fran, Kremer Leonor, Mellström Britt, Naranjo Jose R (Sep. 2002). Ca2+-dependent block of CREB-CBP transcription by repressor DREAM. EMBO J. 21 (17): 4583–92 (England)​. ISSN:0261-4189. PMID:12198160. PMC:126180. DOI:10.1093/emboj/cdf440.
  33. Li, S, Aufiero B, Schiltz R L, Walsh M J (Jun. 2000). Regulation of the homeodomain CCAAT displacement/cut protein function by histone acetyltransferases p300/CREB-binding protein (CBP)-associated factor and CBP. Proc. Natl. Acad. Sci. U.S.A. 97 (13): 7166–71 (UNITED STATES)​. ISSN:0027-8424. PMID:10852958. PMC:16517. DOI:10.1073/pnas.130028697.
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  35. Zhao, Fang, McCarrick-Walmsley Ruth, Akerblad Peter, Sigvardsson Mikael, Kadesch Tom (Jun. 2003). Inhibition of p300/CBP by early B-cell factor. Mol. Cell. Biol. 23 (11): 3837–46 (United States)​. ISSN:0270-7306. PMID:12748286. PMC:155219. DOI:10.1128/MCB.23.11.3837-3846.2003.
  36. a b Sheppard, H M, Harries J C, Hussain S, Bevan C, Heery D M (Jan. 2001). Analysis of the steroid receptor coactivator 1 (SRC1)-CREB binding protein interaction interface and its importance for the function of SRC1. Mol. Cell. Biol. 21 (1): 39–50 (UNITED STATES)​. ISSN:0270-7306. PMID:11113179. PMC:86566. DOI:10.1128/MCB.21.1.39-50.2001.
  37. Chakraborty, S, Senyuk V, Sitailo S, Chi Y, Nucifora G (Nov. 2001). Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. J. Biol. Chem. 276 (48): 44936–43 (United States)​. ISSN:0021-9258. PMID:11568182. DOI:10.1074/jbc.M106733200.
  38. Nasrin, N, Ogg S, Cahill C M, Biggs W, Nui S, Dore J, Calvo D, Shi Y, Ruvkun G, Alexander-Bridges M C (Sep. 2000). DAF-16 recruits the CREB-binding protein coactivator complex to the insulin-like growth factor binding protein 1 promoter in HepG2 cells. Proc. Natl. Acad. Sci. U.S.A. 97 (19): 10412–7 (UNITED STATES)​. ISSN:0027-8424. PMID:10973497. PMC:27038. DOI:10.1073/pnas.190326997.
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